Growth of the non-photosynthetic bacterium Pseudomonas MA on methylamine causes the induction of at least three enzymes: N- methylglutamate synthetase, N-methylglutamate dehydrogenase, and 5- hydroxy N-methly pyroglutamate synthetase. The first of these enzymes is a flavoprotein which forms a reduced flavin-glutarl enzyme. Research is currently involved in determining the nature of the covalent linkage of the glutarl moiety to the enzyme. The enzyme, 5-hydroxy N- methyl pyroglutamate synthetase, catalyzes the reversible formation of a number of alpha-ketoglutaryl gamma-amides. Kinetic evidence leads to the proposal of an alpha-ketoglutaryl enzyme intermediate in this reaction. Current efforts are being focused on providing additional evidence to support this conclusion. Partitioning experiments, in which the ratio of hydrolysis to amide formation is measured for various ester and amide substrates, will be used to confirm the alpha-ketoglutaryl intermediate. In conjuction with the above research, the involvement of the three enzymes mentioned above in one-carbon metabolism is being studied. Preliminary data suggests that N-methylglutamate synthetase is a carrier of one-carbon units, and the N-methly glutamate dehydrogenase reaction (N-methylglutamate yields glutamate plus formaldehyde) serves to activate the methyl group for further metabolism. At present we can find no function for the 5-hydroxy N-methyl pyroglutamate synthetase reaction.